| Project/Area Number |
13670583
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Gastroenterology
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| Research Institution | Institute for Developmental Research, Aichi Human Service Center |
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Principal Investigator |
INAGUMA Yutaka Institute for Developmental Research, Department of Biochemistry, Senior Researcher, 究所・生化学部, 主任研究員 (10250250)
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| Co-Investigator(Kenkyū-buntansha) |
ITO Hidenori Institute for Developmental Research, Department of Biochemistry, Researcher, 究所・生化学部, 研究員 (40311443)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2002: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2001: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | SUMO / Ubiquitin / DNA repair / APEX / TTRAP / transcriotion / 核移行シグナル |
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| Research Abstract |
SUMO-1 (Small Ubiquitin-related Modifier-1) was detected at a high level in rat pancreas by Western blot analyses. Similarly SUMO-2 existed in the same organ. We observed that acinar cells presented strong positive by immunohistochemistry. SUMO-2 responded to heat stress by forming high molecular weight complex. To investigate a role of SUMO-2, we carried out an yeast two-hybrid method with SUMO-2gg as a bait and repetively identified TTRAP (TRAP and TNF receptor-associated protein). We obtained two sorts of cDNA with different start positions of 5' coding region and different positions of 3' non-coding region. PSORT program predicted a nuclear localization signal (KKRR) in the N-terminal region. Tagged TTRAP expressed in COS cells localized in the nucleus. Mutation of the NLS resulted in loss of nuclear localization. TTRAP conserved APE-1 domain which is involved in DNA repair and regulation of transcription. Purifird TTRAP cleaved AP-site efficiently but not 8-oxo-dG sequences. The cleavage of AP-site was inhibited by addtion of EDTA indicating that this reaction was dependent on Mg^<2+>. TTRAP also interacted with Ubc9 and p53. Taken together with the structure and localization of TTRAP, it is suggested that TTRAP involves in DNA repair or transcription regulation in the nucleus.
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